Abstract

O-Mannosylation is suggested to be essential for protein secretion in
Trichoderma reesei. In protein O-glycosylation, the first mannosyl residue is
transferred to a serine or threonine hydroxyl group of the protein from
dolichyl phosphate mannose by protein O-mannosyltransferase. In Saccharomyces
cerevisiae, seven PMT genes have been cloned coding for these enzymes. In the
present work, the characterisation of the pmt1 cDNA from T. reesei is
reported. Sequence analysis of the predicted protein revealed the highest
similarity to Schizosaccharomyces pombe Pmt and to Pmt4p of Saccharomyces
cerevisiae. In contrast, expression of the T. reesei cDNA in various S.
cerevisiae pmt mutants showed functional similarity to the yeast Pmt2 protein.

abstract = "O-Mannosylation is suggested to be essential for protein secretion in Trichoderma reesei. In protein O-glycosylation, the first mannosyl residue is transferred to a serine or threonine hydroxyl group of the protein from dolichyl phosphate mannose by protein O-mannosyltransferase. In Saccharomyces cerevisiae, seven PMT genes have been cloned coding for these enzymes. In the present work, the characterisation of the pmt1 cDNA from T. reesei is reported. Sequence analysis of the predicted protein revealed the highest similarity to Schizosaccharomyces pombe Pmt and to Pmt4p of Saccharomyces cerevisiae. In contrast, expression of the T. reesei cDNA in various S. cerevisiae pmt mutants showed functional similarity to the yeast Pmt2 protein.",

N2 - O-Mannosylation is suggested to be essential for protein secretion in
Trichoderma reesei. In protein O-glycosylation, the first mannosyl residue is
transferred to a serine or threonine hydroxyl group of the protein from
dolichyl phosphate mannose by protein O-mannosyltransferase. In Saccharomyces
cerevisiae, seven PMT genes have been cloned coding for these enzymes. In the
present work, the characterisation of the pmt1 cDNA from T. reesei is
reported. Sequence analysis of the predicted protein revealed the highest
similarity to Schizosaccharomyces pombe Pmt and to Pmt4p of Saccharomyces
cerevisiae. In contrast, expression of the T. reesei cDNA in various S.
cerevisiae pmt mutants showed functional similarity to the yeast Pmt2 protein.

AB - O-Mannosylation is suggested to be essential for protein secretion in
Trichoderma reesei. In protein O-glycosylation, the first mannosyl residue is
transferred to a serine or threonine hydroxyl group of the protein from
dolichyl phosphate mannose by protein O-mannosyltransferase. In Saccharomyces
cerevisiae, seven PMT genes have been cloned coding for these enzymes. In the
present work, the characterisation of the pmt1 cDNA from T. reesei is
reported. Sequence analysis of the predicted protein revealed the highest
similarity to Schizosaccharomyces pombe Pmt and to Pmt4p of Saccharomyces
cerevisiae. In contrast, expression of the T. reesei cDNA in various S.
cerevisiae pmt mutants showed functional similarity to the yeast Pmt2 protein.